文献类型：期刊文献

英文题名：Heterologous expression of chaperones from hyperthermophilic archaea inhibits aminoglycoside-induced protein misfolding in Escherichia coli

作者：Peng, S.[1];Chu, Z.[2,3];Lu, J.[2,3];Li, D.[2,3];Wang, Y.[1];Yang, S.[2,3];Zhang, Y.[2,3]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China;[3]Chinese Acad Sci, Key Lab Synthet Biol, Shanghai 200032, Peoples R China

年份：2017

卷号：82

期号：10

起止页码：1169

外文期刊名：BIOCHEMISTRY-MOSCOW

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000412949900009)】；

基金：This work was supported by National Basic Research Program of China (973 Program) (project No. 2012CB721103).

语种：英文

外文关键词：aminoglycoside; protein mistranslation; Escherichia coli; hyperthermophilic archaeon; Pyrococcus furiosus; chaperone

摘要：Aminoglycoside antibiotics affect protein translation fidelity and lead to protein aggregation and an increase in intracellular oxidative stress level as well. The overexpression of the chaperonin GroEL/GroES system promotes short-term tolerance to aminoglycosides in Escherichia coli. Here, we demonstrated that the coexpression of prefoldin or Hsp60 originating from the hyperthermophilic archaeon Pyrococcus furiosus in E. coli cells can rescue cell growth and inhibit protein aggregation induced by streptomycin exposure. The results of our study show that hyperthermophilic chaperones endow E. coli with a higher tolerance to streptomycin than the GroEL/GroES system, and that they exert better effects on the reduction of intracellular protein misfolding, indicating that these chaperones have unique features and functions.